Yoshizawa S, Fourmy D, Puglisi J D
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.
Science. 1999 Sep 10;285(5434):1722-5. doi: 10.1126/science.285.5434.1722.
Translational fidelity is established by ribosomal recognition of the codon-anticodon interaction within the aminoacyl-transfer RNA (tRNA) site (A site) of the ribosome. Experiments are presented that reveal possible contacts between 16S ribosomal RNA and the codon-anticodon complex. N1 methylation of adenine at position 1492 (A1492) and A1493 interfered with A-site tRNA binding. Mutation of A1492 and A1493 to guanine or cytosine also impaired A-site tRNA binding. The deleterious effects of A1492G or A1493G (or both) mutations were compensated by 2'fluorine substitutions in the mRNA codon. The results suggest that the ribosome recognizes the codon-anticodon complex by adenine contacts to the messenger RNA backbone and provide a mechanism for molecular discrimination of correct versus incorrect codon-anticodon pairs.
翻译保真度是通过核糖体对核糖体氨酰基转移RNA(tRNA)位点(A位点)内密码子-反密码子相互作用的识别来建立的。本文展示的实验揭示了16S核糖体RNA与密码子-反密码子复合物之间可能存在的接触。腺嘌呤第1492位(A1492)和A1493位的N1甲基化干扰了A位点tRNA的结合。将A1492和A1493突变为鸟嘌呤或胞嘧啶也会损害A位点tRNA的结合。A1492G或A1493G(或两者)突变的有害影响可通过mRNA密码子中的2'氟取代来补偿。结果表明,核糖体通过腺嘌呤与信使RNA主链的接触来识别密码子-反密码子复合物,并提供了一种分子机制来区分正确与错误的密码子-反密码子对。